ArticleNature communications2015
Conserved Omp85 lid-lock structure and substrate recognition in FhaC.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 36 citations in OpenAlex.
- DeepPath: overcoming data scarcity for protein transition pathway prediction using physics-based deep learning.Chemical science · 2026Article
- First inhibitor of a bacterial two-partner secretion system.bioRxiv : the preprint server for biology · 2026Article
- Leptospira interrogans encodes a canonical BamA and three novel noNterm Omp85 outer membrane protein paralogs.Scientific reports · 2024Article
- Article
- Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.International journal of molecular sciences · 2023Review
- Characterization of synthetic antigen binding fragments targeting Toc75 for the isolation of TOC in A. thaliana and P. sativum.Structure (London, England : 1993) · 2023Article
- Filamentous Hemagglutinin ofInternational journal of molecular sciences · 2022Article
- Genomic erosion and horizontal gene transfer shape functional differences of the ExlA toxin iniScience · 2022Article
- Functional and Structural Diversity of Bacterial Contact-Dependent Growth Inhibition Effectors.Frontiers in molecular biosciences · 2022Review
- Large-Scale Conformational Changes of FhaC Provide Insights Into the Two-Partner Secretion Mechanism.Frontiers in molecular biosciences · 2022Article
- Plasticity within the barrel domain of BamA mediates a hybrid-barrel mechanism by BAM.Nature communications · 2021Article
- Protein import and export across the bacterial outer membrane.Current opinion in structural biology · 2021Review
- Structural insight into toxin secretion by contact-dependent growth inhibition transporters.eLife · 2020Article
- Membrane thinning and lateral gating are consistent features of BamA across multiple species.PLoS computational biology · 2020Article
- Structural insight into mitochondrial β-barrel outer membrane protein biogenesis.Nature communications · 2020Article
- C-terminal kink formation is required for lateral gating in BamA.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Applications of sequence coevolution in membrane protein biochemistry.Biochimica et biophysica acta. Biomembranes · 2018Review
- Membrane protein insertion through a mitochondrial β-barrel gate.Science (New York, N.Y.) · 2018Article
- The POTRA domains of Toc75 exhibit chaperone-like function to facilitate import into chloroplasts.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structural snapshots of the β-barrel assembly machinery.The FEBS journal · 2017Review
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Omp85 proteins mediate translocation of polypeptide substrates across and into cellular membranes. They share a common architecture comprising substrate-interacting POTRA domains, a C-terminal 16-stranded β-barrel pore and two signature motifs located on the inner barrel wall and at the tip of the extended L6 loop. The observation of two distinct conformations of the L6 loop in the available Omp85 structures previously suggested a functional role of conformational changes in L6 in the Omp85 mechanism. Here we present a 2.5 Å resolution structure of a variant of the Omp85 secretion protein FhaC, in which the two signature motifs interact tightly and form the conserved 'lid lock'. Reanalysis of previous structural data shows that L6 adopts the same, conserved resting state position in all available Omp85 structures. The FhaC variant structure further reveals a competitive mechanism for the regulation of substrate binding mediated by the linker to the N-terminal plug helix H1.
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